ID   SOPB_ECOLI              Reviewed;         323 AA.
AC   P62558; P08867;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 85.
DE   RecName: Full=Protein SopB;
DE   AltName: Full=Plasmid partition protein B;
GN   Name=sopB; Synonyms=B; OrderedLocusNames=ECOK12F047;
OS   Escherichia coli (strain K12).
OG   Plasmid F.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=3029390; DOI=10.1016/0022-2836(86)90459-6;
RA   Mori H., Kondo A., Ohshima A., Ogura T., Hiraga S.;
RT   "Structure and function of the F plasmid genes essential for
RT   partitioning.";
RL   J. Mol. Biol. 192:1-15(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Eichenlaub R.;
RT   "F plasmid DNA complete mini-F region (F coordinates 40.301F to 49.869F).";
RL   Submitted (AUG-1986) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / CR63;
RA   Shimizu H., Saitoh Y., Suda Y., Uehara K., Sampei G., Mizobuchi K.;
RT   "Complete nucleotide sequence of the F plasmid: its implications for
RT   organization and diversification of plasmid genomes.";
RL   Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Control of plasmid partitioning; required to recognize the
CC       cis-acting. Binds specifically with the DNA segment containing the sopC
CC       region. SopB is trans-acting.
CC   -!- MISCELLANEOUS: Overproduction of SopB protein causes IncG
CC       incompatibility.
CC   -!- SIMILARITY: Belongs to the ParB family. {ECO:0000305}.
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DR   EMBL; X04619; CAA28296.1; -; Genomic_DNA.
DR   EMBL; M12987; AAA24903.1; -; Genomic_DNA.
DR   EMBL; AP001918; BAA97917.1; -; Genomic_DNA.
DR   PIR; T00244; T00244.
DR   RefSeq; NP_061426.1; NC_002483.1.
DR   RefSeq; WP_000817031.1; NZ_SSUW01000063.1.
DR   PDB; 3KZ5; X-ray; 1.58 A; A/B/E=276-323.
DR   PDB; 3MKW; X-ray; 2.99 A; B/P=155-272.
DR   PDB; 3MKY; X-ray; 2.86 A; B/P=155-323.
DR   PDB; 3MKZ; X-ray; 2.98 A; A/B/N/U=155-272.
DR   PDBsum; 3KZ5; -.
DR   PDBsum; 3MKW; -.
DR   PDBsum; 3MKY; -.
DR   PDBsum; 3MKZ; -.
DR   AlphaFoldDB; P62558; -.
DR   SMR; P62558; -.
DR   EvolutionaryTrace; P62558; -.
DR   PRO; PR:P62558; -.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0030541; P:plasmid partitioning; IEA:UniProtKB-KW.
DR   CDD; cd16394; sopB_N; 1.
DR   DisProt; DP02863; -.
DR   Gene3D; 1.10.10.2830; -; 1.
DR   Gene3D; 6.10.140.1550; -; 1.
DR   InterPro; IPR004437; ParB/RepB/Spo0J.
DR   InterPro; IPR003115; ParB/Sulfiredoxin_dom.
DR   InterPro; IPR036086; ParB/Sulfiredoxin_sf.
DR   InterPro; IPR040873; SoPB_HTH.
DR   NCBIfam; TIGR00180; parB_part; 1.
DR   PANTHER; PTHR38973:SF2; PARB_SULFIREDOXIN DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR38973; PLASMID PARTITIONING CONTROL PROTEIN-RELATED; 1.
DR   Pfam; PF02195; ParBc; 1.
DR   Pfam; PF18090; SoPB_HTH; 1.
DR   SMART; SM00470; ParB; 1.
DR   SUPFAM; SSF110849; ParB/Sulfiredoxin; 1.
PE   1: Evidence at protein level;
KW   3D-structure; DNA-binding; Plasmid; Plasmid partition.
FT   CHAIN           1..323
FT                   /note="Protein SopB"
FT                   /id="PRO_0000068408"
FT   DNA_BIND        180..199
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000250"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   HELIX           160..172
FT                   /evidence="ECO:0007829|PDB:3MKY"
FT   TURN            173..177
FT                   /evidence="ECO:0007829|PDB:3MKY"
FT   HELIX           179..186
FT                   /evidence="ECO:0007829|PDB:3MKY"
FT   HELIX           190..201
FT                   /evidence="ECO:0007829|PDB:3MKY"
FT   HELIX           204..208
FT                   /evidence="ECO:0007829|PDB:3MKY"
FT   STRAND          210..212
FT                   /evidence="ECO:0007829|PDB:3MKY"
FT   HELIX           213..215
FT                   /evidence="ECO:0007829|PDB:3MKY"
FT   HELIX           218..227
FT                   /evidence="ECO:0007829|PDB:3MKY"
FT   TURN            228..230
FT                   /evidence="ECO:0007829|PDB:3MKY"
FT   HELIX           232..247
FT                   /evidence="ECO:0007829|PDB:3MKY"
FT   HELIX           254..263
FT                   /evidence="ECO:0007829|PDB:3MKY"
FT   HELIX           267..269
FT                   /evidence="ECO:0007829|PDB:3MKY"
FT   STRAND          278..282
FT                   /evidence="ECO:0007829|PDB:3KZ5"
FT   STRAND          285..290
FT                   /evidence="ECO:0007829|PDB:3KZ5"
FT   STRAND          293..299
FT                   /evidence="ECO:0007829|PDB:3KZ5"
FT   TURN            300..302
FT                   /evidence="ECO:0007829|PDB:3KZ5"
FT   HELIX           305..318
FT                   /evidence="ECO:0007829|PDB:3KZ5"
SQ   SEQUENCE   323 AA;  35372 MW;  3CC19C873CED3C1C CRC64;
     MKRAPVIPKH TLNTQPVEDT SLSTPAAPMV DSLIARVGVM ARGNAITLPV CGRDVKFTLE
     VLRGDSVEKT SRVWSGNERD QELLTEDALD DLIPSFLLTG QQTPAFGRRV SGVIEIADGS
     RRRKAAALTE SDYRVLVGEL DDEQMAALSR LGNDYRPTSA YERGQRYASR LQNEFAGNIS
     ALADAENISR KIITRCINTA KLPKSVVALF SHPGELSARS GDALQKAFTD KEELLKQQAS
     NLHEQKKAGV IFEAEEVITL LTSVLKTSSA SRTSLSSRHQ FAPGATVLYK GDKMVLNLDR
     SRVPTECIEK IEAILKELEK PAP
//